Key result
Binding of full-length myosin VI to cargo adaptor proteins optineurin or truncated Dab2 induces internal dimerization, reducing ATPase activity to 2.6/sec per head and enabling processive movement.
Population
Full-length myosin VI (in vitro model)
Comparison
Cargo adaptor proteins vs Myosin VI in isolation
Design
Preclinical
Authors
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Supports myosin VI dimerization as a cellular design feature; extends motor protein models but leaves open cardiac validation.
Absolute Event Rate: 2.6% vs 4.6%
Cargo binding exposes internal dimerization sequences within full-length myosin VI, suggesting it is designed to function as a dimer in cells.
Phichith et al. (2009) studied this question. Cargo adaptor proteins (optineurin and truncated Dab2) vs. Full-length myosin VI alone was evaluated on Actin-activated ATPase activity (Vmax, ATP hydrolyzed per head per second). Binding of full-length myosin VI to cargo adaptor proteins optineurin or truncated Dab2 induces internal dimerization, reducing ATPase activity to 2.6/sec per head and enabling processive movement.
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